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(Shanghai, China). Serum proteomics was performed to identify circulating factors associated with serum-induced GLS1 activity in NRVMs. Serum samples from 40 randomly selected PD patients were processed for LC-MS/MS-based label-free proteomic analysis. High-abundance serum proteins were depleted before digestion. Serum proteins were denatured in SDT buffer, reduced with DTT, alkylated with iodoacetamide, and digested using filter-aided sample preparation. Briefly, 200 μg protein per sample was loaded onto 30-kDa ultrafiltration devices, washed with UA buffer to remove detergent and low-molecular-weight contaminants, alkylated with 100 mM iodoacetamide in the dark for 30 min, and washed sequentially with UA buffer and 0.1 M TEAB. Proteins were digested overnight at 37°C with sequencing-grade trypsin at a 1:50 enzyme-to-protein ratio, and the resulting peptides were collected and quantified by UV absorbance at 280 nm. For DIA analysis, 200 ng peptides from each sample were mixed with iRT standards, desalted on Evotips, and analyzed on an Evosep One system coupled to a timsTOF Pro mass spectrometer equipped with a CaptiveSpray ion source. Peptides were separated on a 15 cm × 150 μm C18 analytical column packed with 1.9 μm beads at 50°C using the Evosep 30 samples-per-day method. Data were acquired in diaPASEF mode using two 25 m/z precursor isolation windows per 100-ms TIMS scan, with 18 scans covering the doubly and triply charged peptide region in the m/z–ion mobility plane. For spectral library generation, pooled peptides were fractionated by high-pH reversed-phase chromatography on an Agilent 1260 Infinity II HPLC using an XBridge Peptide BEH C18 column. Fractions were collected at 1-min intervals, dried by vacuum centrifugation, desalted on Evotips, and analyzed on the same LC-MS/MS platform in DDA-PASEF mode. DDA spectra were acquired over an m/z range of 100–1700 and an ion mobility range of 0.75–1.40 1/K0, with 10 MS/MS scans per cycle, 100-ms ramp time, 0.4-min active exclusion, and 42 eV collision energy. Raw DDA and DIA files were processed using Spectronaut. Spectra were searched against the UniProt human protein database (Uniprot_HomoSapiens_20377_20220308_swissprot) with trypsin specified as the digestion enzyme. Carbamidomethylation of cysteine was set as a fixed modification, whereas methionine oxidation and protein N-terminal acetylation were set as variable modifications. Precursor- and protein-level q-value cutoffs were set to 1%. DIA data were analyzed using dynamic iRT calibration, Spectronaut’s default extraction settings, and the mutated decoy strategy. Protein quantities were calculated from the average intensity of the top three filtered peptides passing the 1% q-value cutoff.PrideNot availableIn this study, 4D-DIA-based proteomic profiling was performed by GeneChem Co., Ltd. (Shanghai, China). Serum proteomics was performed to identify circulating factors associated with serum-induced GLS1 activity in NRVMs. Serum samples from 40 randomly selected PD patients were processed for LC-MS/MS-based label-free proteomic analysis. High-abundance serum proteins were depleted before digestion. Serum proteins were denatured in SDT buffer, reduced with DTT, alkylated with iodoacetamide, and digested using filter-aided sample preparation. Briefly, 200 μg protein per sample was loaded onto 30-kDa ultrafiltration devices, washed with UA buffer to remove detergent and low-molecular-weight contaminants, alkylated with 100 mM iodoacetamide in the dark for 30 min, and washed sequentially with UA buffer and 0.1 M TEAB. Proteins were digested overnight at 37°C with sequencing-grade trypsin at a 1:50 enzyme-to-protein ratio, and the resulting peptides were collected and quantified by UV absorbance at 280 nm. For DIA analysis, 200 ng peptides from each sample were mixed with iRT standards, desalted on Evotips, and analyzed on an Evosep One system coupled to a timsTOF Pro mass spectrometer equipped with a CaptiveSpray ion source. Peptides were separated on a 15 cm × 150 μm C18 analytical column packed with 1.9 μm beads at 50°C using the Evosep 30 samples-per-day method. Data were acquired in diaPASEF mode using two 25 m/z precursor isolation windows per 100-ms TIMS scan, with 18 scans covering the doubly and triply charged peptide region in the m/z–ion mobility plane. For spectral library generation, pooled peptides were fractionated by high-pH reversed-phase chromatography on an Agilent 1260 Infinity II HPLC using an XBridge Peptide BEH C18 column. Fractions were collected at 1-min intervals, dried by vacuum centrifugation, desalted on Evotips, and analyzed on the same LC-MS/MS platform in DDA-PASEF mode. DDA spectra were acquired over an m/z range of 100–1700 and an ion mobility range of 0.75–1.40 1/K0, with 10 MS/MS scans per cycle, 100-ms ramp time, 0.4-min active exclusion, and 42 eV collision energy. Raw DDA and DIA files were processed using Spectronaut. Spectra were searched against the UniProt human protein database (Uniprot_HomoSapiens_20377_20220308_swissprot) with trypsin specified as the digestion enzyme. Carbamidomethylation of cysteine was set as a fixed modification, whereas methionine oxidation and protein N-terminal acetylation were set as variable modifications. Precursor- and protein-level q-value cutoffs were set to 1%. DIA data were analyzed using dynamic iRT calibration, Spectronaut’s default extraction settings, and the mutated decoy strategy. Protein quantities were calculated from the average intensity of the top three filtered peptides passing the 1% q-value cutoff.ProteomicsJunnan WuDepartment of Nephrology, Zhejiang University Medical College Affiliated Sir Run Run Shaw Hospital, Qingchun Road 3rd, Hangzhou 310000, Zhejiang Province, ChinaPARTIALHomo Sapiens (human)wjhjdd@163.comNot availableDepartment of Nephrology, Zhejiang University Medical College Affiliated Sir Run Run Shaw Hospital, Qingchun Road 3rd, Hangzhou 310000, Zhejiang Province, China.ChinafalseProteomic analysis of CKD-associated left ventricular hypertrophyLeft ventricular hypertrophy (LVH) is critical in chronic kidney disease (CKD), but its mechanisms remain unclear. This study employed multi-omics approaches, including RNA-seq and integrated metabolomics, to characterize metabolic alterations in cardiomyocytes (CM) of CKD mice, revealing enhanced glutaminolysis and impaired oxidative phosphorylation. We identified that glutaminase 1 (GLS1), the rate-limiting enzyme of glutaminolysis, is significantly upregulated and enzymatically activated in CM under CKD conditions. A multi-center cohort study confirmed that serum-induced GLS1 activity was associated with LV hypertrophic remodeling. Cardiomyocyte-specific deletion or pharmacological inhibition of GLS1 attenuated CKD-induced cardiac hypertrophy. Proteomic analysis revealed that multiple circulating proteins in the serum of CKD patients are associated with GLS1 enzymatic activity. Furthermore, phosphate (Pi), a representative uremic toxin, functions as a critical modulator of GLS1 activity and expression, compromising mitochondrial bioenergetics by promoting ammonia production and reducing mitochondrially encoded respiratory chain proteins. These integrated metabolic effects underscore the pivotal role of GLS1 in orchestrating myocardial energy reprogramming, thereby contributing to CKD-induced LVH.2026-09-302026-05-03PXD077955NEWT:6945NEWT:3555NEWT:2NEWT:157546NEWT:35554NEWT:38942NEWT:307972NEWT:32046NEWT:544496NEWT:2042546NEWT:45351NEWT:43179NEWT:4513NEWT:5722NEWT:376741NEWT:55153NCBITaxon:10407NEWT:1736309NEWT:1211601NEWT:876138NEWT:557436NEWT:237561NEWT:5833NEWT:6928NEWT:10036NEWT:36745NEWT:1351NEWT:1438992NEWT:2649997NEWT:272563NEWT:79220NEWT:224326NCBITaxon:79857NEWT:1096976NEWT:95648NEWT:3885NEWT:3888NEWT:1589NEWT:135622NEWT:6915NEWT:3649NEWT:101510NEWT:3880NEWT:272559NEWT:3641NEWT:383379NEWT:10029NEWT:1000589NEWT:85962NEWT:317447NEWT:7955NEWT:7959NEWT:2261NEWT:31156NEWT:4565NEWT:1264690NEWT:515619NEWT:192875NEWT:34305NEWT:59729NCBITaxon:183674NEWT:224308NEWT:84645NEWT:626528NEWT:139927NEWT:4558NEWT:209285NEWT:211586NEWT:1283NEWT:931281NEWT:4550NEWT:1000561NEWT:197NCBITaxon:79824NEWT:4787NCBITaxon:4563NEWT:5755NEWT:44689NEWT:3218NEWT:5759NEWT:1736231NEWT:1270NEWT:2242NEWT:4784NEWT:11320NEWT:360106NEWT:287NEWT:10117NEWT:10239NEWT:10116NEWT:1280NEWT:1735272NEWT:83334NEWT:83332NEWT:44685NEWT:317513NEWT:1148NEWT:580240NEWT:294128NEWT:11676NEWT:55571NEWT:100226NEWT:4530NEWT:4896NEWT:75058NEWT:13616NEWT:1094343NEWT:296543NEWT:1773NEWT:1895NEWT:1182590NEWT:935293NEWT:64152NEWT:4924NEWT:749200NEWT:990346NEWT:145953NEWT:257309NEWT:100816NEWT:263NEWT:230741NEWT:52283NEWT:284812NCBITaxon:1313NEWT:43330NEWT:408169NEWT:44544NEWT:4911NEWT:645463NEWT:3702NEWT:129249NEWT:990119NEWT:408172NEWT:408170NEWT:493760NEWT:260710NEWT:257313NEWT:400772NEWT:3708NEWT:128161NEWT:332648NEWT:106592NEWT:536231NEWT:1432138NEWT:10312NEWT:1424507NCBITaxon:1773NEWT:9598NEWT:8030NEWT:1639NEWT:188229NEWT:3818NEWT:480NEWT:4909NEWT:67767NEWT:432359NEWT:46835NEWT:2711NEWT:376686NEWT:95486NEWT:9103NEWT:29159NEWT:10306NCBITaxon:2759NEWT:1233435NEWT:8022NEWT:145943NCBITaxon:4932NEWT:595536NEWT:240906NEWT:593117NEWT:3635NEWT:5811NEWT:235443NEWT:2719099NEWT:411483NEWT:884019NEWT:198215NEWT:411490NEWT:983964NEWT:169963NEWT:499175NEWT:476272NEWT:3747NEWT:367830NEWT:178616NEWT:410289NEWT:373153NEWT:352472NEWT:360094NEWT:470NEWT:1313NEWT:411469NEWT:84023NEWT:559292NCBITaxon:5811NEWT:411464NEWT:411460NEWT:2762NEWT:1174673NEWT:562NEWT:411470NEWT:33952NEWT:2094720NCBITaxon:2697049NEWT:28038NEWT:1423NEWT:4932NEWT:3603NEWT:2759NEWT:3847NEWT:327159NEWT:178876NEWT:327160NEWT:573NEWT:9031NEWT:7091NEWT:241368NEWT:42528NEWT:190802NEWT:9778NEWT:150475NEWT:9417NEWT:7111NEWT:347515NEWT:1216979NEWT:5180NEWT:256737NEWT:115104NEWT:1081927NEWT:1238993NEWT:67825NEWT:185579NEWT:13076NEWT:1249668NEWT:317NEWT:7227NEWT:7469NEWT:885318NEWT:9402NEWT:415540NEWT:4081NEWT:554NEWT:98334NEWT:426428NEWT:7574NEWT:7215NEWT:575412NEWT:29204NEWT:2172103NEWT:507601NCBITaxon:6157NEWT:746360NEWT:6239NEWT:470150NEWT:216257NEWT:9986NEWT:4054NEWT:73239NEWT:226186NEWT:1268063NEWT:8782NEWT:1263854NEWT:435590NEWT:1902NEWT:160488NEWT:28104NCBITaxon:2NEWT:985076NEWT:1215323NEWT:623NEWT:52641NEWT:7038NEWT:6192NEWT:28532NCBITaxon:38727NEWT:2829NEWT:216599NEWT:216595NEWT:243230NEWT:8355NEWT:9685NEWT:7029NEWT:1080772NEWT:1283300NEWT:6183NEWT:6063NEWT:334747NEWT:61235NEWT:6289NEWT:436486NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:725NEWT:170187NEWT:260707NCBITaxon:6191NEWT:1836NEWT:185431NEWT:29760NEWT:260704NEWT:703612NEWT:260705NEWT:80863NEWT:2697049NCBITaxon:6073NEWT:884204NEWT:6279NEWT:1123869NEWT:9544NEWT:7370NEWT:83906NEWT:607699NEWT:6282NEWT:426688NEWT:208964NEWT:1134506NEWT:575584NEWT:38783NEWT:8727NEWT:4006NEWT:8726NEWT:6426NEWT:6669NEWT:10090NEWT:4120NEWT:51515NEWT:5693NEWT:8724NEWT:51511NEWT:92867NEWT:8723NEWT:5334NEWT:37334NEWT:382352NCBITaxon:10359NEWT:242619NEWT:632957NEWT:373995NEWT:5689NEWT:544404NEWT:9925NEWT:8839NEWT:4232NEWT:2758385NEWT:4113NEWT:837NEWT:11298NEWT:171101NEWT:714NEWT:421932NEWT:196627NEWT:5691NEWT:48479NEWT:627025NEWT:1097677NEWT:242507NEWT:61674NEWT:1117957NEWT:9913NEWT:4100NEWT:1076NEWT:6763NEWT:3498NEWT:803NEWT:29722NEWT:380394NEWT:1692259NEWT:180066NEWT:135588NEWT:1843183NEWT:58002NEWT:326423NEWT:4577NEWT:1416333NEWT:5664NEWT:2157NEWT:749906NEWT:418985NEWT:146479NEWT:1911079NCBITaxon:620NEWT:264203NEWT:1480154NEWT:1274414NEWT:27606NEWT:59202NEWT:9975NEWT:9612NEWT:38865NEWT:51953NEWT:3197NEWT:9615NEWT:10299NEWT:860688NEWT:36329NEWT:1147787NCBITaxon:3044782NEWT:72407NEWT:349741NEWT:9605NEWT:9606NEWT:157295NEWT:641501NEWT:7668NEWT:915099NEWT:74940NEWT:9721NEWT:137221NEWT:1450511NEWT:1143193NEWT:411901NEWT:9838NEWT:105884NCBITaxon:9615NEWT:58334NEWT:1193501NEWT:3055NEWT:6326NEWT:6689NEWT:5476NEWT:1274432NEWT:1274426NEWT:70448NEWT:9825NEWT:1274423NEWT:393765NEWT:698936NEWT:39946NEWT:9823NEWT:9940NEWT:521001NEWT:39947NEWT:1274420NEWT:578458